Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5506979 | Biochemistry and Biophysics Reports | 2017 | 8 Pages |
â¢H10 binds to CT-DNA with a favorable entropy change.â¢H10-G binding site size was found to be 7 bp in titrations of CT-DNA.â¢H10 binding to CT-DNA was accompanied by a negative heat capacity change.â¢Dehydration of the H10-DNA complex is the principle contributor to the favorable entropy change.
Linker histones (H1) are the basic proteins in higher eukaryotes that are responsible for the final condensation of chromatin. In contrast to the nucleosome core histone proteins, the role of H1 in compacting DNA is not clearly understood. In this study ITC was used to measure the binding constant, enthalpy change, and binding site size for the interactions of H10, or its C-terminal (H10-C) and globular (H10-G) domains to highly polymerized calf-thymus DNA at temperatures from 288Â K to 308Â K. Heat capacity changes, ÎCp, for these same H10 binding interactions were estimated from the temperature dependence of the enthalpy changes. The enthalpy changes for binding H10, H10-C, or H10-G to CT-DNA are all endothermic at 298Â K, becoming more exothermic as the temperature is increased. The ÎH for binding H10-G to CT-DNA is exothermic at temperatures above approximately 300Â K. Osmotic stress experiments indicate that the binding of H10 is accompanied by the release of approximately 35 water molecules.We estimate from our naked DNA titration results that the binding of the H10 to the nucleosome places the H10 protein in close contact with approximately 41 DNA bp. The breakdown is that the H10 carboxyl terminus interacts with 28Â bp of linker DNA on one side of the nucleosome, the H10 globular domain binds directly to 7Â bp of core DNA, and shields another 6 linker DNA bases, 3Â bp on either side of the nucleosome where the linker DNA exits the nucleosome core.